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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5240
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pubmed:dateCreated |
1995-12-28
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pubmed:databankReference |
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pubmed:abstractText |
A yeast two-hybrid system was used to identify a protein that interacts with and enhances the human progesterone receptor (hPR) transcriptional activity without altering the basal activity of the promoter. Because the protein stimulated transactivation of all the steroid receptors tested, it has been termed steroid receptor coactivator-1 (SRC-1). Coexpression of SRC-1 reversed the ability of the estrogen receptor to squelch activation by hPR. Also, the amino terminal truncated form of SRC-1 acted as a dominant-negative repressor. Together, these results indicate that SRC-1 encodes a coactivator that is required for full transcriptional activity of the steroid receptor superfamily.
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pubmed:grant |
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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cyclic AMP Response...,
http://linkedlifedata.com/resource/pubmed/chemical/Histone Acetyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Hormone Antagonists,
http://linkedlifedata.com/resource/pubmed/chemical/Mifepristone,
http://linkedlifedata.com/resource/pubmed/chemical/Promegestone,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Progesterone,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Steroid,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0036-8075
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
24
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pubmed:volume |
270
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1354-7
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pubmed:dateRevised |
2010-4-26
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pubmed:meshHeading |
pubmed-meshheading:7481822-Amino Acid Sequence,
pubmed-meshheading:7481822-Base Sequence,
pubmed-meshheading:7481822-Cyclic AMP Response Element-Binding Protein,
pubmed-meshheading:7481822-Gene Expression,
pubmed-meshheading:7481822-HeLa Cells,
pubmed-meshheading:7481822-Histone Acetyltransferases,
pubmed-meshheading:7481822-Hormone Antagonists,
pubmed-meshheading:7481822-Humans,
pubmed-meshheading:7481822-Mifepristone,
pubmed-meshheading:7481822-Molecular Sequence Data,
pubmed-meshheading:7481822-Nuclear Receptor Coactivator 1,
pubmed-meshheading:7481822-Promegestone,
pubmed-meshheading:7481822-Receptors, Progesterone,
pubmed-meshheading:7481822-Receptors, Steroid,
pubmed-meshheading:7481822-Recombinant Fusion Proteins,
pubmed-meshheading:7481822-Trans-Activators,
pubmed-meshheading:7481822-Transcription Factors,
pubmed-meshheading:7481822-Transcriptional Activation,
pubmed-meshheading:7481822-Transfection
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pubmed:year |
1995
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pubmed:articleTitle |
Sequence and characterization of a coactivator for the steroid hormone receptor superfamily.
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pubmed:affiliation |
Department of Cell Biology, Baylor College of Medicine, Houston, TX 77030, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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